|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-469 |
1.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQL-----QAE-------MSQKLQHfKEVEVAKIKME----EKAQTQKEISELRYELER--THQAKAEALVSREK 217
Cdd:COG1196 195 LGELERQLeplerQAEkaeryreLKEELKE-LEAELLLLKLReleaELEELEAELEELEAELEEleAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEIEAKEVYAQRQS---LLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY 294
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 295 DQKLKtELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNK 374
Cdd:COG1196 354 EEAEA-ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 375 QNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES 454
Cdd:COG1196 433 LEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
330
....*....|....*
gi 2024343403 455 HKQFLEKQLQSEVER 469
Cdd:COG1196 510 VKAALLLAGLRGLAG 524
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
148-448 |
1.43e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRkEIEKQLQAEMSQKLQHFKEVEVAKikmEEKAQTQKEISELRYELER-----THQAKAEALVSREKNAIER 222
Cdd:COG1196 227 AELLLLKLR-ELEAELEELEAELEELEAELEELE---AELAELEAELEELRLELEElelelEEAQAEEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTel 302
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-- 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 303 lkyQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 382
Cdd:COG1196 381 ---LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 383 LKEVSDyPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV 448
Cdd:COG1196 458 EEALLE-LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
187-507 |
1.94e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 187 KAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQE--IEAKEVYAQRQSLLKDIEVMRTReaELKQRIEAFEI 264
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaERYKELKAELRELELALLVLRLE--ELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 265 TQKLQEEKNKTIDDALRRREVAVkNIEETYDQKLKTELLKYQLELKEEYIartnkvtedekknkekamllreeavAVNSK 344
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALAN-------------------------EISRL 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 345 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 424
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEELESLEAELEELEAELEELESRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 425 SQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEkQLQSEVERSAQLKTQLLD--SEATVRKLNVQVEDLKLQLKQTQ 502
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLE-RLEDRRERLQQEIEELLKklEEAELKELQAELEELEEELEELQ 453
|
....*
gi 2024343403 503 AALEN 507
Cdd:TIGR02168 454 EELER 458
|
|
| LisH_2 |
pfam16045 |
LisH; |
27-52 |
1.98e-10 |
|
LisH;
Pssm-ID: 464992 Cd Length: 28 Bit Score: 56.31 E-value: 1.98e-10
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
120-412 |
1.71e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 120 YRESLAEKLQLIDEQFADsypqhhkyepLEGKLHEYRKEIEkQLQAEMSQ-KLQHFKEVEVAKIKMEEKAQTQKEISELR 198
Cdd:COG1196 233 KLRELEAELEELEAELEE----------LEAELEELEAELA-ELEAELEElRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 199 YELERTHQAKAEALVSREKNAIERLQKQQEIEAKEvyAQRQSLLKDIEvmrTREAELKQRIEAFEITQKLQEEKNKTIDD 278
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELE--EELEELEEELE---EAEEELEEAEAELAEAEEALLEAEAELAE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 279 ALRRREVAVKNIEEtydqkLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKEL 358
Cdd:COG1196 377 AEEELEELAEELLE-----ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2024343403 359 ELDLESVKAQVLLVNKQNQLLTEKLKEVSDyplLKEEKLELQVQNKLLRQQLDE 412
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAE---LLEELAEAAARLLLLLEAEAD 502
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-541 |
5.07e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 5.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 125 AEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE---KAQTQKEISELRYEL 201
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakkKAEEAKKADEAKKKA 1479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 202 ErtHQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEvmRTREAELKQRIEAFEITQKLQEEKNKTIDDALR 281
Cdd:PTZ00121 1480 E--EAKKADEA---KKKAEEAKKKADEAKKAAEAKKKADEAKKAE--EAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 282 RREvAVKNIEEtydqKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVnsKKEELKQAvsrtKELELD 361
Cdd:PTZ00121 1553 KAE-ELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--KAEEAKKA----EEAKIK 1621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLR--DKLSQPSAEHLACQA-EL 438
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALKKEAeEA 1701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 439 RKVEHSRRLVMDEFESHKQfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDL-KLQLKQTQAALENEVYRNPKPSL 517
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKkKIAHLKKEEEKKAEEIRKEKEAV 1780
|
410 420
....*....|....*....|....
gi 2024343403 518 VDRSVIDLIDDRIVPHDVYTDSIF 541
Cdd:PTZ00121 1781 IEEELDEEDEKRRMEVDKKIKDIF 1804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
144-506 |
7.78e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.70 E-value: 7.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKqLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELertHQAKAEALVsREKNAIERL 223
Cdd:TIGR02169 171 KKEKALEELEEVEENIER-LDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYE---LLKEKEALE-RQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 224 QKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRI------EAFEITQKLQEEKNK--TIDDALRRREVAVKNIEETyD 295
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQLRVKEKIGELEAEiaSLERSIAEKERELEDAEER-L 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 296 QKLKTELLKYQLELK------EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSK----KEELKQAVSRTKELELDLESV 365
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEelereiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfaetRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 366 KAQVLLVNKQNQLLTEKLKEV-SDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHS 444
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLnAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024343403 445 RRLVMDEFEShkqfLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR02169 485 LSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
151-487 |
1.13e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 151 KLHEYRKEIEKQLQA-------------EMSQKLQHFK-EVEVAKIKMEEKAQ-TQKEISELRYELERTHQAKAEALVSR 215
Cdd:TIGR02168 169 KYKERRKETERKLERtrenldrledilnELERQLKSLErQAEKAERYKELKAElRELELALLVLRLEELREELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 216 EKNAIERLQKQQEIEAKEvyaqrqsllKDIEVMRTREAELKQRIE----AFEITQKLQEEKNKTIDDALRRREVAVKNIE 291
Cdd:TIGR02168 249 KEAEEELEELTAELQELE---------EKLEELRLEVSELEEEIEelqkELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 292 ETYDQKL----KTELLKYQLELKEEYIARTNKVTED-EKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVK 366
Cdd:TIGR02168 320 ELEAQLEelesKLDELAEELAELEEKLEELKEELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 367 AQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELqvQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRR 446
Cdd:TIGR02168 400 NEIERLEARLERLEDRRER------LQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2024343403 447 LVMDEFESHKQFLEkQLQSEVERSAQLKTQLLDSEATVRKL 487
Cdd:TIGR02168 472 EAEQALDAAERELA-QLQARLDSLERLQENLEGFSEGVKAL 511
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
144-523 |
4.27e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.46 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKA---EALVSREKNAI 220
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKkadEAKKAEEAKKA 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 221 ERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETY-----D 295
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMklyeeE 1604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 296 QKLKTELLKYQLELKEEyiARTNKVTEDEKKNKEKAMLLREEAVavnSKKEELKQAvsrtkelELDLESVKAQVLLVNKQ 375
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEK---KKAEELKKA-------EEENKIKAAEEAKKAEE 1672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 376 NQLLTEKLKevsdypllKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESH 455
Cdd:PTZ00121 1673 DKKKAEEAK--------KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343403 456 KQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVedLKLQLKQTQAALENEVYRNPKPSLVDRSVI 523
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
189-500 |
4.30e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.37 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 189 QTQKEISELRYELERThQAKAEALvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKL 268
Cdd:TIGR02168 674 ERRREIEELEEKIEEL-EEKIAEL---EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 269 QEEkNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELK-EEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE 347
Cdd:TIGR02168 750 AQL-SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 348 LKQAVSRTK----ELELDLESVKAQVLLVNKQ-NQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRD 422
Cdd:TIGR02168 829 LERRIAATErrleDLEEQIEELSEDIESLAAEiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403 423 KLSQPSAEHLACQAELRKVEhsrrLVMDEFESHKQFLEKQLQSEVERSAQ-LKTQLLDSEATVRKLNVQVEDLKLQLKQ 500
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
124-387 |
7.83e-08 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 56.40 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 124 LAEKLQLIDEQFADSYPQHHKYEP-LEGKLHEYRKEIEKQLQ-----AEMSQKLQHFKEVEVAKIKMEEKAQTQK----- 192
Cdd:PLN03229 484 LQERLENLREEFSKANSQDQLMHPvLMEKIEKLKDEFNKRLSrapnyLSLKYKLDMLNEFSRAKALSEKKSKAEKlkaei 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 193 -----------EISE----LRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVYaqrQSLLKDIEVMRTREAELKQ 257
Cdd:PLN03229 564 nkkfkevmdrpEIKEkmeaLKAEVASSGASSGDELDDDLKEKVEKMKKEIELELAGVL---KSMGLEVIGVTKKNKDTAE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 258 RIEAFEITQK---LQEEKNKTIDDALRrrevavknieeTYDQKLKTELLKyqLELKEEyiARTNKVTEDEKKNKEKAMLL 334
Cdd:PLN03229 641 QTPPPNLQEKiesLNEEINKKIERVIR-----------SSDLKSKIELLK--LEVAKA--SKTPDVTEKEKIEALEQQIK 705
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2024343403 335 REEAVAVNSKkeELKQavsrtKELELDLESVKAQVLLVNKQNQLLTEKLKEVS 387
Cdd:PLN03229 706 QKIAEALNSS--ELKE-----KFEELEAELAAARETAAESNGSLKNDDDKEED 751
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-481 |
8.73e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 151 KLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELerthqakAEALVSREKNAIERLQKQQEIE 230
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLL-------YLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 231 AKEVYAQRQSLLKDIEVMRTREAELKQRIEAfeitQKLQEEKNKTIDDAL------RRREVAVKNIEETYDQKLKTELLK 304
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKE----KKLQEEELKLLAKEEeelkseLLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 305 YQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESvKAQVLLVNKQNQLLTEKLK 384
Cdd:pfam02463 326 AEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLES-ERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 385 EVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQ 464
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-ELKKSEDLLKETQLVK 481
|
330
....*....|....*..
gi 2024343403 465 SEVERSAQLKTQLLDSE 481
Cdd:pfam02463 482 LQEQLELLLSRQKLEER 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-387 |
1.57e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 141 QHHKYEPLEGKLHEY---RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVS 214
Cdd:TIGR02168 237 LREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 215 REKNAIERLQ--KQQEIEAKEVYAQRQsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEE 292
Cdd:TIGR02168 317 QLEELEAQLEelESKLDELAEELAELE---EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 293 T-YDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLL 371
Cdd:TIGR02168 394 QiASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-LKELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
250
....*....|....*.
gi 2024343403 372 VNKQNQLLTEKLKEVS 387
Cdd:TIGR02168 473 AEQALDAAERELAQLQ 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
122-477 |
1.59e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.37 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 122 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLqAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYEL 201
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEY 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 202 ERTHQaKAEALVSREKNAIERLQKQ-QEIEAKEvyAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNK------ 274
Cdd:PRK03918 306 LDELR-EIEKRLSRLEEEINGIEERiKELEEKE--ERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrlt 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 275 --TIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKeeyIARTNKVTEDEKKNK-------------EKAMLLREEAV 339
Cdd:PRK03918 383 glTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE---IKELKKAIEELKKAKgkcpvcgrelteeHRKELLEEYTA 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 340 AVNSKKEELKQAVSRTKELELDLESVKAqvlLVNKQNQLLteKLKEVSDYPLLKEEKLElqvqnKLLRQQLDETRTENQH 419
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEK---VLKKESELI--KLKELAEQLKELEEKLK-----KYNLEELEKKAEEYEK 529
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2024343403 420 LRDKLSQPSAEHLACQAELRKVEhsrrlvmdEFESHKQFLEKQLQSEVERSAQLKTQL 477
Cdd:PRK03918 530 LKEKLIKLKGEIKSLKKELEKLE--------ELKKKLAELEKKLDELEEELAELLKEL 579
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-479 |
1.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 184 MEEKAQTQKEISELRYELERTHQ-------------AKAEALVSREKNAIERLQK-QQEIEAKEvyAQRQSLLKDIEVMR 249
Cdd:TIGR02169 694 QSELRRIENRLDELSQELSDASRkigeiekeieqleQEEEKLKERLEELEEDLSSlEQEIENVK--SELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 250 TREAELKQRIEAFE------ITQKLQEEKNKtIDDALRRREVAVKNIE---------ETYDQKLKTELLKYQLELKEEYI 314
Cdd:TIGR02169 772 EDLHKLEEALNDLEarlshsRIPEIQAELSK-LEEEVSRIEARLREIEqklnrltleKEYLEKEIQELQEQRIDLKEQIK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 315 ARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvNKQNQLLTEKLKEVSDYPLLKE 394
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE------RKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 395 EKLELQVQNKLLRQQLDETRTENQHLRDkLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLeKQLQSEVERSAQLK 474
Cdd:TIGR02169 925 KLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEER 1002
|
....*
gi 2024343403 475 TQLLD 479
Cdd:TIGR02169 1003 KAILE 1007
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
159-470 |
2.64e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 159 IEKQLQAEMSQKLQHFKEVEVAKIKmEEKAQTQKEIsELRYELERTHQAKAEAL-------VSREKNAIERLQKQQEIEA 231
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLR-QEKEEKAREV-ERRRKLEEAEKARQAEMdrqaaiyAEQERMAMERERELERIRQ 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 232 KEvyaqrqsllKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA--VKNIEETYDQKLKTELLKYQLEL 309
Cdd:pfam17380 356 EE---------RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAArkVKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 310 KEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDY 389
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 390 PLLKEEKLELQVQNKLLRQQL----DETRTENQHLRDKlSQPSAEHLACQAELRKVEHSRRLvMDEFESHKQFLEKQLQS 465
Cdd:pfam17380 507 AMIEEERKRKLLEKEMEERQKaiyeEERRREAEEERRK-QQEMEERRRIQEQMRKATEERSR-LEAMEREREMMRQIVES 584
|
....*
gi 2024343403 466 EVERS 470
Cdd:pfam17380 585 EKARA 589
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
253-508 |
4.44e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 4.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 253 AELKQRIEAFEItQKLQEEKNKTIDDALRRREV--AVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEK 330
Cdd:COG1196 196 GELERQLEPLER-QAEKAERYRELKEELKELEAelLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 331 AMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKaqvllvnKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQL 410
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLE-------ERRRELEERLEE------LEEELAELEEELEELEEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 411 DETRTENQHLRDKLSQPSAEHLACQAELRKVE---HSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKL 487
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEAEaelAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419
|
250 260
....*....|....*....|.
gi 2024343403 488 NVQVEDLKLQLKQTQAALENE 508
Cdd:COG1196 420 EEELEELEEALAELEEEEEEE 440
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-508 |
5.45e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKQLQaEMSQKLQHFKEVE-VAKIKMEEKAQTQKEISELRYELERTHQAKAEalVSREKNAIER 222
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEeLIKEKEKELEEVLREINEISSELPELREELEK--LEKEVKELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQkqQEIEAKEVyaQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTEL 302
Cdd:PRK03918 236 LK--EEIEELEK--ELESLEGSKRKLEEKIRELEERIE--ELKKEIEELEEK------------VKELKELKEKAEEYIK 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 303 LKyqlELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEK 382
Cdd:PRK03918 298 LS---EFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 383 LKevsdyplLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSAEhlacQAELRKVEHSRRLVMDEFESHKQF--LE 460
Cdd:PRK03918 375 ER-------LKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITAR----IGELKKEIKELKKAIEELKKAKGKcpVC 441
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 461 KQLQSEVERS---AQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 508
Cdd:PRK03918 442 GRELTEEHRKellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKE 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
149-359 |
6.64e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 6.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE--KAQTQKEISELRY--ELERTHQAKAEALV-SREKNAIERL 223
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEakKAEEERNNEEIRKfeEARMAHFARRQAAIkAEEARKADEL 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 224 QKQQEIEAKEvYAQRQSLLKDIEVMRTREAELKQRIEA---FEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKT 300
Cdd:PTZ00121 1284 KKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAkkkAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403 301 ELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE 359
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
148-506 |
6.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVakiKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQ 227
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEE---ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQ- 306
Cdd:COG4717 124 LLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEe 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 307 LELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQA-------------VSRTKELELDLESVKAQVLLV- 372
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallalLGLGGSLLSLILTIAGVLFLVl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 373 ----------NKQNQLLTEKLKEVSDYPLLKE-EKLELQVQNKLLRQQLDETRTENQHLRDKLSQ-----PSAEHLACQA 436
Cdd:COG4717 284 gllallflllAREKASLGKEAEELQALPALEElEEEELEELLAALGLPPDLSPEELLELLDRIEElqellREAEELEEEL 363
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403 437 ELRKVEHSRRLVMDEF--ESHKQFLEK-----QLQSEVERSAQLKTQLLDSEATVRKLNVQV--EDLKLQLKQTQAALE 506
Cdd:COG4717 364 QLEELEQEIAALLAEAgvEDEEELRAAleqaeEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
91-500 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 91 LMWILMGLTEHHLSKECNDRETQTISIPpyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIE--KQLQAEMS 168
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKP---ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 169 QKLQHFKEVEVAKIKMEEKAQTQKEISEL--RYE-LERTHQAKAEALVSREKNAIERLQKQQEIEAK------EVYAQRQ 239
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAELAELpeRLEeLEERLEELRELEEELEELEAELAELQEELEELleqlslATEEELQ 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 240 SLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIARTNK 319
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 320 ------------VTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRT--KELELDLESVKAQVLLVNKQNQLLTEKLKE 385
Cdd:COG4717 276 agvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEEllAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 386 VSDYpllkEEKLELQVQNKLLRQQLDETRTENqhlRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQS 465
Cdd:COG4717 356 AEEL----EEELQLEELEQEIAALLAEAGVED---EEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430
....*....|....*....|....*....|....*.
gi 2024343403 466 EV-ERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQ 500
Cdd:COG4717 429 ELeEELEELEEELEELEEELEELREELAELEAELEQ 464
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
185-512 |
3.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 185 EEKAQTQKEISELRYELERTHQakaealvsrEKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEI 264
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQS---------ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 265 TQKLQEEKNKTIDDALRRREvavKNIEEtydqkLKTELLKYQLELkeeyiartnkvtedekkNKEKAMLLREEAVAVNSK 344
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELE---ARIEE-----LEEDLHKLEEAL-----------------NDLEARLSHSRIPEIQAE 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 345 KEELKQAVSRtkeLELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEKLELQVQNKLLRQQLDETRTENQHLRDKL 424
Cdd:TIGR02169 800 LSKLEEEVSR---IEARLREIEQKLNRLTLEKEYLEKEIQE------LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 425 sqpsAEHlacQAELRKVEHSRrlvmdefeshkqfleKQLQSEVERsaqLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAA 504
Cdd:TIGR02169 871 ----EEL---EAALRDLESRL---------------GDLKKERDE---LEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
....*...
gi 2024343403 505 LENEVYRN 512
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
156-297 |
4.71e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.76 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAK--- 232
Cdd:TIGR02794 83 QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEA--EAERKAKEEAAKQAEEEAKaka 160
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403 233 --EVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYDQK 297
Cdd:TIGR02794 161 aaEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
266-420 |
7.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 266 QKLQEEKNKTIDDALRRREVAVKNIEetydQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKK 345
Cdd:PRK12704 34 KEAEEEAKRILEEAKKEAEAIKKEAL----LEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 346 EELKQAVSRTKELELDLESVKAQV-LLVNKQNQllteKLKEVSDypLLKEEklelqVQNKLLRQQLDETRTENQHL 420
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELeELIEEQLQ----ELERISG--LTAEE-----AKEILLEKVEEEARHEAAVL 174
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
149-313 |
9.62e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAEmsqklqhfkEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQ---- 224
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEA---------KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEnldr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 225 KQQEIEAKE--VYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTIDDAlrrREVAVKNIEEtydqKLKTEL 302
Cdd:PRK12704 101 KLELLEKREeeLEKKEKELEQKQQELEKKEEELEELIE--EQLQELERISGLTAEEA---KEILLEKVEE----EARHEA 171
|
170
....*....|.
gi 2024343403 303 LKYQLELKEEY 313
Cdd:PRK12704 172 AVLIKEIEEEA 182
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-495 |
1.62e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRK---EIEKQLqAEMSQKLQHFKE-VEVAKIKMEEKAQTQKEISELRYELERTHQ-AKAEALVSREKN 218
Cdd:PRK03918 294 EYIKLSEFYEEYLDelrEIEKRL-SRLEEEINGIEErIKELEEKEERLEELKKKLKELEKRLEELEErHELYEEAKAKKE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 219 AIERLQKQQEIEAKEvyaqrqSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNktiddalrRREVAVKNIEETYDQKL 298
Cdd:PRK03918 373 ELERLKKRLTGLTPE------KLEKELEELEKAKEEIEEEIS--KITARIGELKK--------EIKELKKAIEELKKAKG 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 299 KTELLKYQL------ELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEE------LKQAVSRTKELE-----LD 361
Cdd:PRK03918 437 KCPVCGRELteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEeklkkYN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLA-CQAELRK 440
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEeLEERLKE 596
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403 441 VE--HSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLK 495
Cdd:PRK03918 597 LEpfYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELE 653
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
100-508 |
1.85e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 100 EHHLSKECNDRETQTISIppyrESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQL---------------- 163
Cdd:TIGR00618 378 TQHIHTLQQQKTTLTQKL----QSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQryaelcaaaitctaqc 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 164 -------QAEMSQKL----QHFKEVEVAKIKMEEK-------AQTQKEI------SELRYELERTHQAKAEALVSREKNA 219
Cdd:TIGR00618 454 eklekihLQESAQSLkereQQLQTKEQIHLQETRKkavvlarLLELQEEpcplcgSCIHPNPARQDIDNPGPLTRRMQRG 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 220 IERLQKQQEIEAKeVYAQRQSLLKDIEVMRTREAELKQRIEAFEIT-QKLQEEKNKTIDDALRRREVAVKNIEEtydQKL 298
Cdd:TIGR00618 534 EQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCdNRSKEDIPNLQNITVRLQDLTEKLSEA---EDM 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 299 KTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLRE-EAVAVNSKKEELKQAVSRTKELELDLesvkaqvllvNKQNQ 377
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAlHALQLTLTQERVREHALSIRVLPKEL----------LASRQ 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 378 LLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFES--- 454
Cdd:TIGR00618 680 LALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvlk 757
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2024343403 455 HKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALENE 508
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
169-402 |
2.03e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 169 QKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERT----------HQAKAEALVSREKNAIERLQKQQEIEAKEVYAQR 238
Cdd:PRK05771 23 EALHELGVVHIEDLKEELSNERLRKLRSLLTKLSEAldklrsylpkLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 239 QSLLKDIEVMRTREAELKQRIEAFEITQKLqeeknkTIDDA-LRRRE---VAVKNIEETYDqklktELLKYQLELKEEYI 314
Cdd:PRK05771 103 KELEEEISELENEIKELEQEIERLEPWGNF------DLDLSlLLGFKyvsVFVGTVPEDKL-----EELKLESDVENVEY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 315 ARTNK-------VTEDEKKNKEKAMLLREEAVAVN-----SKKEELKQAVSRTKELELDLESVKAQvllvnkqnqlLTEK 382
Cdd:PRK05771 172 ISTDKgyvyvvvVVLKELSDEVEEELKKLGFERLEleeegTPSELIREIKEELEEIEKERESLLEE----------LKEL 241
|
250 260
....*....|....*....|
gi 2024343403 383 LKEVSDYPLLKEEKLELQVQ 402
Cdd:PRK05771 242 AKKYLEELLALYEYLEIELE 261
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
146-507 |
3.20e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 146 EPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVeVAKIKMEEKAQTQKeISELRYELE------------RTHQAKAEA-- 211
Cdd:pfam12128 271 ETLIASRQEERQETSAELNQLLRTLDDQWKEK-RDELNGELSAADAA-VAKDRSELEaledqhgafldaDIETAAADQeq 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 212 --LVSREKNAIER-----LQKQQEIEAKevYAQRQSLLK-----DIEVMR-----TREAELKQRIEAFEITQKLQEEKNK 274
Cdd:pfam12128 349 lpSWQSELENLEErlkalTGKHQDVTAK--YNRRRSKIKeqnnrDIAGIKdklakIREARDRQLAVAEDDLQALESELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 275 TIDDALRRREVAVKNIEET-------YDQKLKTELLKYQLELKEEYIARTNKvtEDEKKNKEKAMLLREEAVA---VNSK 344
Cdd:pfam12128 427 QLEAGKLEFNEEEYRLKSRlgelklrLNQATATPELLLQLENFDERIERARE--EQEAANAEVERLQSELRQArkrRDQA 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 345 KEELKQAVSRTKELELDLESVKAQvlLVNKQNQLLTEKLKEVSDYpllKEEKLELQVQNKLLRQQLDETRTEnqhlrdkl 424
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQ--LFPQAGTLLHFLRKEAPDW---EQSIGKVISPELLHRTDLDPEVWD-------- 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 425 SQPSAEH--LACQAELRKVEHSRRLVM-DEFESHKQFLEKQLQSEVERSAQLKTQLLdseatvrKLNVQVEDLKLQLKQT 501
Cdd:pfam12128 572 GSVGGELnlYGVKLDLKRIDVPEWAASeEELRERLDKAEEALQSAREKQAAAEEQLV-------QANGELEKASREETFA 644
|
....*.
gi 2024343403 502 QAALEN 507
Cdd:pfam12128 645 RTALKN 650
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-507 |
3.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIE---KQLQAEMSQKLQHF-KEVEVAKIKMEEK-AQTQKEISELRYELERTHQAKAEALVSREKNAIER 222
Cdd:TIGR04523 286 LEKQLNQLKSEISdlnNQKEQDWNKELKSElKNQEKKLEEIQNQiSQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQKQQEIEakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKNI-EETYDQKLKTE 301
Cdd:TIGR04523 366 EEKQNEIE--KLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLkETIIKNNSEIK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 302 LLKYQLELKEEYIARTNKVTEDEKKNKEKAML--------LREEAVAVNSKKEELKQAVSRTKELELDLESVKAQV-LLV 372
Cdd:TIGR04523 444 DLTNQDSVKELIIKNLDNTRESLETQLKVLSRsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIsSLK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 373 NKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKllRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVehsrrlvMDEF 452
Cdd:TIGR04523 524 EKIEKLESEKKEKESKISDLEDELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQEL-------IDQK 594
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2024343403 453 ESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALEN 507
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQ 649
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
145-474 |
3.41e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 145 YEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRyeleRTHQAKAEALVSREKNAIERLQ 224
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEAR----KAEDAKRVEIARKAEDARKAEE 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 225 KQQEIEAKEVYAQRqsllKDIEVMRT---REAELKQRIEA---FEITQKLQE----EKNKTIdDALRRREVAVKNIEETY 294
Cdd:PTZ00121 1169 ARKAEDAKKAEAAR----KAEEVRKAeelRKAEDARKAEAarkAEEERKAEEarkaEDAKKA-EAVKKAEEAKKDAEEAK 1243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 295 ---DQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTK----------ELELD 361
Cdd:PTZ00121 1244 kaeEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkaeeakkadEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQnqllTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKV 441
Cdd:PTZ00121 1324 AEEAKKKADAAKKK----AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
330 340 350
....*....|....*....|....*....|...
gi 2024343403 442 EHSRRLVMDEFEshKQFLEKQLQSEVERSAQLK 474
Cdd:PTZ00121 1400 AEEDKKKADELK--KAAAAKKKADEAKKKAEEK 1430
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-506 |
3.43e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIE---KQLQAEMSQKL-------QHFKEVEVAKIKMEEKAQTQKE-ISELRYELERTHQAKAEALVSREKnaiER 222
Cdd:pfam01576 650 EAKEELErtnKQLRAEMEDLVsskddvgKNVHELERSKRALEQQVEEMKTqLEELEDELQATEDAKLRLEVNMQA---LK 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 223 LQKQQEIEAKEVYAQ--RQSLLKDIEVMRT-REAELKQRIEAFEITQKLQ---EEKNKTIDDALRRREVAVKNIeetydQ 296
Cdd:pfam01576 727 AQFERDLQARDEQGEekRRQLVKQVRELEAeLEDERKQRAQAVAAKKKLEldlKELEAQIDAANKGREEAVKQL-----K 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 297 KLKTELLKYQLELKEEYIAR-----TNKVTEDEKKNKEKAMLLREEAVAVNSKKEelKQAVSRTKEL--ELDLESVKAQV 369
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRdeilaQSKESEKKLKNLEAELLQLQEDLAASERAR--RQAQQERDELadEIASGASGKSA 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 370 LLVNKQN------QLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEH 443
Cdd:pfam01576 880 LQDEKRRleariaQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEG 959
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024343403 444 SRR----LVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam01576 960 TVKskfkSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAE 1026
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
148-387 |
3.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 148 LEGKLHEYRKEIEkqlQAEmsQKLQHFKE----VEVAkikmEEKAQTQKEISELRYELERTHQAKAEAlvsreKNAIERL 223
Cdd:COG3206 180 LEEQLPELRKELE---EAE--AALEEFRQknglVDLS----EEAKLLLQQLSELESQLAEARAELAEA-----EARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 224 QKQQEIEAKEVYAQRQSLLkdIEVMRTREAELKQRIEafEITQKLQEEkNKTIDDALRRREVAvknieetyDQKLKTELL 303
Cdd:COG3206 246 RAQLGSGPDALPELLQSPV--IQQLRAQLAELEAELA--ELSARYTPN-HPDVIALRAQIAAL--------RAQLQQEAQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 304 KYQLELKEEYIArtnkvtedekknkekamlLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKL 383
Cdd:COG3206 313 RILASLEAELEA------------------LQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRL 374
|
....
gi 2024343403 384 KEVS 387
Cdd:COG3206 375 EEAR 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-494 |
4.70e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 235
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 236 AQRQSLLKDIEVMRTREAELKQRIEAfEITQKLQEEKNKTIDDALRRREVAVKNIEET----YDQKLKTELLKYQLELKE 311
Cdd:COG1196 517 AGLRGLAGAVAVLIGVEAAYEAALEA-ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARG 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 312 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL 391
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 392 LKEEKLELQVQ-----NKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLVMDEFESHKQFLEKQLQSE 466
Cdd:COG1196 676 EAEAELEELAErlaeeELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
330 340
....*....|....*....|....*...
gi 2024343403 467 VERSAQLKTQlldsEATVRKLNVQVEDL 494
Cdd:COG1196 756 LPEPPDLEEL----ERELERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
144-495 |
4.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 144 KYEPLEGKLHEYRKEIEKQLQ------AEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREK 217
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKeleekeERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 218 NAIERLQKQQEieakEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQ--------KLQEEKNKTIddaLRRREVAVKN 289
Cdd:PRK03918 391 KELEELEKAKE----EIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrELTEEHRKEL---LEEYTAELKR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 290 IEETY------DQKLKTELLKYQLELKEEYIARTNKVTEDE----------------KKNKEKAMLLREEAVAVNSKKEE 347
Cdd:PRK03918 464 IEKELkeieekERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleelEKKAEEYEKLKEKLIKLKGEIKS 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 348 LKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEV--SDYPLLKEEKLELQ------VQNKLLRQQLDETRTENQH 419
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfESVEELEERLKELEpfyneyLELKDAEKELEREEKELKK 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 420 LRDKLSQPSAEHLACQAELRKV-----EHSRRLVMDEFESHKQF---LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQV 491
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELrkeleELEKKYSEEEYEELREEyleLSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
....
gi 2024343403 492 EDLK 495
Cdd:PRK03918 704 EERE 707
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
124-388 |
5.47e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 124 LAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELER 203
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 204 THQAKAEALVSREKNAIERLQKQQEIEAKEVyaqrqsllkdiEVMRTREAELKQRIEAFeitqKLQEEKNKTIDDALRRR 283
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-----------EELKKKEAEEKKKAEEL----KKAEEENKIKAEEAKKE 1738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 284 EvavkniEEtydQKLKTELLKYQLELKeeyiartNKVTEDEKKNKEKAMLLREEAVAV---NSKKEELKQAVSRTKELEl 360
Cdd:PTZ00121 1739 A------EE---DKKKAEEAKKDEEEK-------KKIAHLKKEEEKKAEEIRKEKEAVieeELDEEDEKRRMEVDKKIK- 1801
|
250 260
....*....|....*....|....*...
gi 2024343403 361 DLESVKAQVLLVNKQNQLLTEKLKEVSD 388
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEMED 1829
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-416 |
5.98e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 185 EEKAQTQKEISELRYELERTHQAKAEALvsREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAfei 264
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALL--KQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 265 tqkLQEEKNKTIDDALRR----REVAVKNIEETYDQKLKTELLKYQLElkeeyiartnkvtedekKNKEKAMLLREEAVA 340
Cdd:COG4942 102 ---QKEELAELLRALYRLgrqpPLALLLSPEDFLDAVRRLQYLKYLAP-----------------ARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 341 VNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKevSDYPLLKEEKLELQVQNKLLRQQLDETRTE 416
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE--KELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
142-506 |
7.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.49 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 142 HHKYEPLEGKLHEYRKEIEKQlqaeMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREkNAIE 221
Cdd:PRK02224 205 HERLNGLESELAELDEEIERY----EEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETERERE-ELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 222 RLQKQQEiEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFeitqklqEEKNKTIDDALRRREVAVKNIEETYDqklkte 301
Cdd:PRK02224 280 EVRDLRE-RLEELEEERDDLLAEAGLDDADAEAVEARREEL-------EDRDEELRDRLEECRVAAQAHNEEAE------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 302 llkyqlelkeeyiartnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAV----SRTKELELDLESVKAQVllvnkqnQ 377
Cdd:PRK02224 346 -----------------SLREDADDLEERAEELREEAAELESELEEAREAVedrrEEIEELEEEIEELRERF-------G 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 378 LLTEKLKEVSDY-PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSaehlaCQAELRKVEHSRRLVMDEfe 453
Cdd:PRK02224 402 DAPVDLGNAEDFlEELREERDELREREAELEatlRTARERVEEAEALLEAGKCPE-----CGQPVEGSPHVETIEEDR-- 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2024343403 454 shkqflekqlqsevERSAQLKTQLLDSEATVRKLNVQVEDLKlQLKQTQAALE 506
Cdd:PRK02224 475 --------------ERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIE 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
121-472 |
8.69e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 121 RESLAEKLQLIDEQFAdsypqhhkyeplegkLHEYRKEIEKQ--LQAEMSQKLQ----HFKEVEVAKIKMEEKAQTQKEI 194
Cdd:COG3096 292 RELFGARRQLAEEQYR---------------LVEMARELEELsaRESDLEQDYQaasdHLNLVQTALRQQEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 195 SELRYELERTHQAKAEALVSREKNAIERLQKQQEI-EAKEVYAQRQSLLkdiEVMRTREAELKQRIEAFEITQKLQEEKN 273
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdSLKSQLADYQQAL---DVQQTRAIQYQQAVQALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 274 KTIDDALRRREVAVKNIEETYDQKLKtelLKYQLELKEEYIARTNKVTE---------DEKKNKEKAMLLREEAVAVNSK 344
Cdd:COG3096 434 LTPENAEDYLAAFRAKEQQATEEVLE---LEQKLSVADAARRQFEKAYElvckiagevERSQAWQTARELLRRYRSQQAL 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 345 KEELKQAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPLLKE------EKLELQVQNKL-----LRQQLDET 413
Cdd:COG3096 511 AQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAeleaqlEELEEQAAEAVeqrseLRQQLEQL 590
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024343403 414 RTENQHLRDK-------------LSQPSAEHLACQAEL-----RKVEHSRRLVM--DEFESHKQflekQLQSEVERSAQ 472
Cdd:COG3096 591 RARIKELAARapawlaaqdalerLREQSGEALADSQEVtaamqQLLEREREATVerDELAARKQ----ALESQIERLSQ 665
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
154-441 |
1.14e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 42.69 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQ----KLQHFKEVEVAKIKMEE---KAQTQKEISELRY--------ELERTHQ-----------A 207
Cdd:NF033838 114 ELTSKTKKELDAAFEQfkkdTLEPGKKVAEATKKVEEaekKAKDQKEEDRRNYptntyktlELEIAESdvevkkaelelV 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 208 KAEALVSREKNAIErlQKQQEIEAKEVYAQRqslLKDIEVMRTR-EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVA 286
Cdd:NF033838 194 KEEAKEPRDEEKIK--QAKAKVESKKAEATR---LEKIKTDREKaEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 287 VKNIEETYDQKlKTELLKYQLELKEEYIARTN-----KVTEDEKKnkekamlLREEAVAVNSKKEELKQAVSRTKELELD 361
Cdd:NF033838 269 VLGEPATPDKK-ENDAKSSDSSVGEETLPSPSlkpekKVAEAEKK-------VEEAKKKAKDQKEEDRRNYPTNTYKTLE 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 362 LESVKAQVLLVNKQNQLLTEKLKEVSDypllkEEKLElQVQNKLLRQQLDETRTENqhLRDKLSQPSAEHLACQAELRKV 441
Cdd:NF033838 341 LEIAESDVKVKEAELELVKEEAKEPRN-----EEKIK-QAKAKVESKKAEATRLEK--IKTDRKKAEEEAKRKAAEEDKV 412
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
152-497 |
2.74e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 152 LHEYRKEIEKQLqaEMSQKLQhfkevevakiKMEEKAQTQKEiselRYELERTHqaKAEALVSREKNAIERLQKQQEIEA 231
Cdd:COG5022 805 LLGSRKEYRSYL--ACIIKLQ----------KTIKREKKLRE----TEEVEFSL--KAEVLIQKFGRSLKAKKRFSLLKK 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 232 KEVYAQRQSLLKDIevmRTREAELKQRIEAFEITQKLQEEKNKTIddalrrrevavknIEETydQKLKTELLKyQLELKE 311
Cdd:COG5022 867 ETIYLQSAQRVELA---ERQLQELKIDVKSISSLKLVNLELESEI-------------IELK--KSLSSDLIE-NLEFKT 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 312 EYIARtnkvtedEKKNKEKAML--LREEAVAVNSKKEELKQAVSRTKELELDLESvkaqvlLVNKQNQLLTEKLKEVSDY 389
Cdd:COG5022 928 ELIAR-------LKKLLNNIDLeeGPSIEYVKLPELNKLHEVESKLKETSEEYED------LLKKSTILVREGNKANSEL 994
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 390 PLLKEEKLELQVQNKLLR---QQLDETRTENQHLRDKLSQPSAEHLACQAELrKVEHSRRLVMDEFESHKQFLeKQLQSE 466
Cdd:COG5022 995 KNFKKELAELSKQYGALQestKQLKELPVEVAELQSASKIISSESTELSILK-PLQKLKGLLLLENNQLQARY-KALKLR 1072
|
330 340 350
....*....|....*....|....*....|..
gi 2024343403 467 VERSAQLKTQLLDSEATVRKLN-VQVEDLKLQ 497
Cdd:COG5022 1073 RENSLLDDKQLYQLESTENLLKtINVKDLEVT 1104
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
126-480 |
2.91e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 126 EKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQlQAEMSQKLQH-----FKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGE-NAESSKRLNEnannlIKQFENTKEKIAEYTKSIDIKKATESL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAKAEALVSREKNAIErlqkqqeieaKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLqEEKNKTIDDAL 280
Cdd:COG5185 315 EEQLAAAEAEQELEESKRETE----------TGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVEL-SKSSEELDSFK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 281 RRREVAVKNIeetyDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELEl 360
Cdd:COG5185 384 DTIESTKESL----DEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREAD- 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 361 dlesvkaqvllvNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNklLRQQLDETRTENQHLRDKLSQPSaehlacqAELRK 440
Cdd:COG5185 459 ------------EESQSRLEEAYDEINRSVRSKKEDLNEELTQ--IESRVSTLKATLEKLRAKLERQL-------EGVRS 517
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2024343403 441 VEHSRRLVMDEFESHKQFLEKQLQSEVERSAQLKTQLLDS 480
Cdd:COG5185 518 KLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAK 557
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
154-511 |
3.08e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEE-KAQTQKEISELRYELERTH---------QAKAEALVSREKNAIERL 223
Cdd:pfam01576 541 EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKtKNRLQQELDDLLVDLDHQRqlvsnlekkQKKFDQMLAEEKAISARY 620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 224 QKQQ---EIEAKEVYAQRQSLLKDIEvmrtreaELKQRIEAFEITQKLQEEKnktIDDALRRREVAVKNIE--------- 291
Cdd:pfam01576 621 AEERdraEAEAREKETRALSLARALE-------EALEAKEELERTNKQLRAE---MEDLVSSKDDVGKNVHelerskral 690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 292 ETYDQKLKTELLKYQLELKEEYIAR------------------TNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVS 353
Cdd:pfam01576 691 EQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVA 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 354 RTKELELDLESVKAQVLLVNKQNQLLTEKLKevsdypllkeeklELQVQNKLLRQQLDETR-------TENQHLRDKLSQ 426
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAANKGREEAVKQLK-------------KLQAQMKDLQRELEEARasrdeilAQSKESEKKLKN 837
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 427 PSAEHLACQAELRKVEHSRRLVMDEFEshkqflekQLQSEVERSAQLKTQLLDSEatvRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERD--------ELADEIASGASGKSALQDEK---RRLEARIAQLEEELEEEQSNTE 906
|
....*..
gi 2024343403 507 --NEVYR 511
Cdd:pfam01576 907 llNDRLR 913
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
393-506 |
3.18e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 393 KEEKL-ELQVQNKLLRQQLDETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLV---MDEFESHKQFLEKQLQSEVE 468
Cdd:PRK09039 51 KDSALdRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELagaGAAAEGRAGELAQELDSEKQ 130
|
90 100 110
....*....|....*....|....*....|....*...
gi 2024343403 469 RSAQLKTQlldseatVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:PRK09039 131 VSARALAQ-------VELLNQQIAALRRQLAALEAALD 161
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
121-502 |
3.44e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 121 RESLAEKLQLIDEQFADSypqhhkyEPLEGKLHEYRKEIEKQLQaEMSQKLQhfKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:pfam01576 42 KNALQEQLQAETELCAEA-------EEMRARLAARKQELEEILH-ELESRLE--EEEERSQQLQNEKKKMQQHIQDLEEQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAKAEalVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELK-QRIEAFEITQKLQEEKNK---TI 276
Cdd:pfam01576 112 LDEEEAARQK--LQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTsNLAEEEEKAKSLSKLKNKheaMI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 277 DDALRRREVAVKNIEETydQKLKTELLKYQLELKEEYIARTNKVTE----DEKKNKE-KAMLLR--EEAVAVNSKKEELK 349
Cdd:pfam01576 190 SDLEERLKKEEKGRQEL--EKAKRKLEGESTDLQEQIAELQAQIAElraqLAKKEEElQAALARleEETAQKNNALKKIR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 350 QAVSRTKELELDLESVKAQVLLVNKQNQLLTEKLKEvsdyplLKEEkLELQVQNKLLRQQLDETR-TENQHLRDKLSQPS 428
Cdd:pfam01576 268 ELEAQISELQEDLESERAARNKAEKQRRDLGEELEA------LKTE-LEDTLDTTAAQQELRSKReQEVTELKKALEEET 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 429 AEHLACQAELRKvEHSRRLV-----MDEFESHKQFLEKQLQSEVERSAQLKTQL-------LDSEATVRKLNVQVEDLKL 496
Cdd:pfam01576 341 RSHEAQLQEMRQ-KHTQALEelteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQA 419
|
....*.
gi 2024343403 497 QLKQTQ 502
Cdd:pfam01576 420 RLSESE 425
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
206-509 |
3.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 206 QAKAEALVSRE--KNAIERLQKQQEIEAKEVYAQR--QSLLKDIEVMRTREAEL-------KQRIEAFEITQKLQEEknk 274
Cdd:COG3206 84 ETQIEILKSRPvlERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGSNVieisytsPDPELAAAVANALAEA--- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 275 TIDDALRRREVAVKNIEETYDQKLKTelLKYQLELKEEYIARTnkvtedekKNKEKAMLLREEAVAVNSKKEELKQAVSr 354
Cdd:COG3206 161 YLEQNLELRREEARKALEFLEEQLPE--LRKELEEAEAALEEF--------RQKNGLVDLSEEAKLLLQQLSELESQLA- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 355 tkELELDLESVKAQVLLVNKQNQLLTEKLKEVSDYPL---LKEEKLELQVQnkllRQQLDETRTEN----QHLRDKLSQp 427
Cdd:COG3206 230 --EARAELAEAEARLAALRAQLGSGPDALPELLQSPViqqLRAQLAELEAE----LAELSARYTPNhpdvIALRAQIAA- 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 428 saehlacqaelrkvehsrrlvmdefeshkqfLEKQLQSEVERS-AQLKTQLLDSEATVRKLNVQVEDLKLQLK------Q 500
Cdd:COG3206 303 -------------------------------LRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAelpeleA 351
|
....*....
gi 2024343403 501 TQAALENEV 509
Cdd:COG3206 352 ELRRLEREV 360
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
135-354 |
3.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 135 FADSYPQHHKYEPLEGKLHEYRKEI---EKQLQAEMSQKLQHFKEVEVAKIKMeekAQTQKEISELRYELERThQAKAEA 211
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIaelEKELAALKKEEKALLKQLAALERRI---AALARRIRALEQELAAL-EAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 212 LVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDD-ALRRREVAVKNI 290
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALRA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024343403 291 EETYDQKLKTELLKYQLELKEEYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSR 354
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
122-475 |
4.79e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 122 ESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQT-QKEISELRYE 200
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAElEEELEEAQEE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAkaealVSREKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFE-------ITQKLQEEKN 273
Cdd:COG4717 222 LEELEEE-----LEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllALLFLLLARE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 274 KTIDDALRRREVAVKNIEETYDQKLKTELLKYQLELKEEYIArtnkVTEDEKKNKEkamlLREEAVAVNSKKEELKQAVS 353
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE----LLELLDRIEE----LQELLREAEELEEELQLEEL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 354 RTKELEL-------DLESVKAQVLLVNKQNQlLTEKLKEVSDY--PLLKEEKLELQVQNK-LLRQQLDETRTENQHLRDK 423
Cdd:COG4717 369 EQEIAALlaeagveDEEELRAALEQAEEYQE-LKEELEELEEQleELLGELEELLEALDEeELEEELEELEEELEELEEE 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2024343403 424 LSQPSAEHLACQAELRKVEHSRRLvmDEFESHKQFLEKQLQSEVERSAQLKT 475
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGEL--AELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
180-356 |
4.84e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 4.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 180 AKIKMEEKAQTQKEISELRYE-----LERT-------HQAKAEALVSREKN----AIERLQKQQEIEAKEVYAQRQSLLK 243
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEarqarLEREkaarearHKKAAEARAAKDKDavaaALARVKAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 244 DIEVMRTREAELKQRIEAFEITQKLQEE--KNKTIDDALRR--------REVAVKNIEETYDQKLKTEL------LKYQL 307
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAAdpKKAAVAAAIARakakkaaqQAANAEAEEEVDPKKAAVAAaiarakAKKAA 595
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 308 ELKEEYIARTNKVTEDEKKNKEKAMLLR------------EEAVAVNSKKEELKQAVSRTK 356
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARakakkaeqqanaEPEEPVDPRKAAVAAAIARAK 656
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
154-357 |
4.90e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 40.56 E-value: 4.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 154 EYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEAlvsREKNAIERLQKQQEIEAKE 233
Cdd:PRK09510 63 QYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQA---EEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 234 VYAQRQSLLKDIEVMrtREAELKQRIEAfeitqklqEEKNKTIDDALRRREV-AVKNIEETYDQKLKTEL-LKYQLELKE 311
Cdd:PRK09510 140 KAAAAAKAKAEAEAK--RAAAAAKKAAA--------EAKKKAEAEAAKKAAAeAKKKAEAEAAAKAAAEAkKKAEAEAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2024343403 312 EYIARTNKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKE 357
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
156-263 |
5.06e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 156 RKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAIERLQKQQEIEAKEVY 235
Cdd:COG1196 673 ALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
90 100
....*....|....*....|....*...
gi 2024343403 236 AQRQSLLKDIEVMRTREAELKQRIEAFE 263
Cdd:COG1196 753 LEELPEPPDLEELERELERLEREIEALG 780
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
121-506 |
5.07e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 121 RESLAEKLQLIdEQFADSYPQ--HHKYEPLEGKLHEYRKEI--EKQLQAEMSQKLQhfkevevakiKMEEKAQTQKEISE 196
Cdd:TIGR00618 196 AELLTLRSQLL-TLCTPCMPDtyHERKQVLEKELKHLREALqqTQQSHAYLTQKRE----------AQEEQLKKQQLLKQ 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 197 LRYELE---------------RTHQAKAEALVSREKNAIERLQKQQEI--EAKEVYAQRQSLLKDIEVMRTREAELKQRI 259
Cdd:TIGR00618 265 LRARIEelraqeavleetqerINRARKAAPLAAHIKAVTQIEQQAQRIhtELQSKMRSRAKLLMKRAAHVKQQSSIEEQR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 260 EAFEITQKLQEEKNKTIDDALRRREVAVKNIEETYD----QKLKTELLKYQLELKEEYIARTNKV----TEDEKKNKEKA 331
Cdd:TIGR00618 345 RLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHihtlQQQKTTLTQKLQSLCKELDILQREQatidTRTSAFRDLQG 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 332 MLLREEAVAVNSKKEELKQAVSRTKELELDLESVKAQVLLVNKQNQlLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLD 411
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 412 -----ETRTENQHLRDKLSQPSAEHLACQAELRKVEHSRRLvmdefeshkQFLEKQLQSEVERSAQLKTQLLDSEATVRK 486
Cdd:TIGR00618 504 cplcgSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSE---------EDVYHQLTSERKQRASLKEQMQEIQQSFSI 574
|
410 420
....*....|....*....|
gi 2024343403 487 LNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR00618 575 LTQCDNRSKEDIPNLQNITV 594
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
161-369 |
5.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 161 KQLQAEMSQKLQHFKEVEvakikmEEKAQTQKEISELRYELERTHQAKAEAlvSREKNAIERLQKQQEIEAKEVYAQRQS 240
Cdd:COG4942 23 AEAEAELEQLQQEIAELE------KELAALKKEEKALLKQLAALERRIAAL--ARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 241 LLKDIEvmrTREAELKQRIEAFEITQKLQEEK----NKTIDDALRRREV------AVKNIEETYDQKLKT-ELLKYQLEL 309
Cdd:COG4942 95 LRAELE---AQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYlkylapARREQAEELRADLAElAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024343403 310 KEEYIARTNKVTEDEKKNKEKAMLLREEAVA-VNSKKEELKQAVSRTKELELDLESVKAQV 369
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLArLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
150-369 |
5.47e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 150 GKLHEYRKEIEKQlQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNA--IERLQKQQ 227
Cdd:PRK02224 478 EELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAaeLEAEAEEK 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIEAFEITQKLQEEKNKTIDDALRRREvAVKNIEETYDQ---KLKT---- 300
Cdd:PRK02224 557 REAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE-KREALAELNDErreRLAEkrer 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 301 -------------ELLKYQLELKEEYIArtnKVTEDEKKNKEKAMLLREEAVAVNSKKEELKQAVSRTKELE---LDLES 364
Cdd:PRK02224 636 kreleaefdeariEEAREDKERAEEYLE---QVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEnrvEALEA 712
|
....*
gi 2024343403 365 VKAQV 369
Cdd:PRK02224 713 LYDEA 717
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
149-506 |
5.86e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAemSQKLQHfkEVEVAKIKMEEKAQTQKE-ISELRYELERTHQAKAEALVSREKNaierlqKQQ 227
Cdd:pfam05483 105 ENKLQENRKIIEAQRKA--IQELQF--ENEKVSLKLEEEIQENKDlIKENNATRHLCNLLKETCARSAEKT------KKY 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 228 EIEAKEVYAQRQSLLKDIEVMRTREAELKQRIE--AFEITQKLQEEKNKtiddalrrrevaVKNIEETYDQKLKTELLKY 305
Cdd:pfam05483 175 EYEREETRQVYMDLNNNIEKMILAFEELRVQAEnaRLEMHFKLKEDHEK------------IQHLEEEYKKEINDKEKQV 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 306 QLELKEeyiartnkVTEDEKKNKEKAMLLREEAVAVNS-------KKEELKQAVSRTKELELDLESVKaqvllVNKQNQL 378
Cdd:pfam05483 243 SLLLIQ--------ITEKENKMKDLTFLLEESRDKANQleektklQDENLKELIEKKDHLTKELEDIK-----MSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 379 LTEKLKEVsdypllkeeklELQVQNKLLRQQLDETRTENQhlrdklsqpsaehlacqaELRKVEHSRRLVMDEFESHKQF 458
Cdd:pfam05483 310 STQKALEE-----------DLQIATKTICQLTEEKEAQME------------------ELNKAKAAHSFVVTEFEATTCS 360
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2024343403 459 LEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-506 |
6.00e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 141 QHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFkEVEVAKIKMEEKAQTQKEISELRYELERTHQAKAEALVSREKNAI 220
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 221 ERLQKQQEIEAKEVYA---QRQSLLKDIEVMRTR--------EAELKQRIEAFEITQKLQEEKNKTIDDALRRREVAVKN 289
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSIltqCDNRSKEDIPNLQNItvrlqdltEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 290 IEEtydQKLKTELLKYQLEL---KEEYIARTNKVTEDEK----KNKEKAMLLREEAVAvnSKKEELKQAVSRTKELELDL 362
Cdd:TIGR00618 639 QEL---ALKLTALHALQLTLtqeRVREHALSIRVLPKELlasrQLALQKMQSEKEQLT--YWKEMLAQCQTLLRELETHI 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 363 E-----------SVKAQVLLVNKQNQLLTEKLKEVSDYPLLKEEKLELQVQNKLLRQQLDETR-TENQHLRDKLSQPSAE 430
Cdd:TIGR00618 714 EeydrefneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTgAELSHLAAEIQFFNRL 793
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024343403 431 HLACQAELRKVEHSRRLVMDEFEshkQFLEKQLQSEVERSAQLKTQLLDSEATVRKLNVQVEDLKLQLKQTQAALE 506
Cdd:TIGR00618 794 REEDTHLLKTLEAEIGQEIPSDE---DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
204-506 |
6.29e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 204 THQAKAEALVSRE--KNAIERLQKQQEIEA-----KEVYAQRQSLLKDIEVMRTREAELKQRIEafEITQKLQEEKNKTi 276
Cdd:PRK11281 27 ARAASNGDLPTEAdvQAQLDALNKQKLLEAedklvQQDLEQTLALLDKIDRQKEETEQLKQQLA--QAPAKLRQAQAEL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 277 dDALRRREVAVKNieetydQKLKTELLKyQLElkeeyiARTNKVTEDEKKnkekamlLREEAVAVNSkkeelkQAVSRTK 356
Cdd:PRK11281 104 -EALKDDNDEETR------ETLSTLSLR-QLE------SRLAQTLDQLQN-------AQNDLAEYNS------QLVSLQT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 357 ELEldlesvKAQVLLVNKQNQL--LTEKLKEVSD--YPLLKEEKLELQVQNKLLRQQLDETRTE---NQHLRDKLSQPSA 429
Cdd:PRK11281 157 QPE------RAQAALYANSQRLqqIRNLLKGGKVggKALRPSQRVLLQAEQALLNAQNDLQRKSlegNTQLQDLLQKQRD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 430 EHLACQAELRK-------VEHSRRLVMDEfESHKQFLEKQ----------LQSEVERSAQLKTQLLdsEATvRKLNVQVE 492
Cdd:PRK11281 231 YLTARIQRLEHqlqllqeAINSKRLTLSE-KTVQEAQSQDeaariqanplVAQELEINLQLSQRLL--KAT-EKLNTLTQ 306
|
330 340
....*....|....*....|.
gi 2024343403 493 DlKLQLK-------QTQAALE 506
Cdd:PRK11281 307 Q-NLRVKnwldrltQSERNIK 326
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-293 |
7.09e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 7.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 121 RESLAEKLQLIDEQFADSYPQHHKYEPLEGKLHEYRKEIEKQLQAEMSQKLQHFKEVEVAKIKMEEKAQTQKEISELRYE 200
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 201 LERTHQAKAEALVS----------REKNAIERLQKQQEIEAKEVYAQRQSLLKDIEVMRTREAELKQR-----------I 259
Cdd:TIGR02168 913 LRRELEELREKLAQlelrleglevRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKikelgpvnlaaI 992
|
170 180 190
....*....|....*....|....*....|....
gi 2024343403 260 EAFEITQKLQEEKNKTIDDALRrrevAVKNIEET 293
Cdd:TIGR02168 993 EEYEELKERYDFLTAQKEDLTE----AKETLEEA 1022
|
|
| LisH |
smart00667 |
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, ... |
27-54 |
7.33e-03 |
|
Lissencephaly type-1-like homology motif; Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.
Pssm-ID: 128913 Cd Length: 34 Bit Score: 35.10 E-value: 7.33e-03
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
149-248 |
8.58e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 39.86 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024343403 149 EGKLHEYRKEIEKQLQAEMSQKLqhfKEVEVAKIKMEEKAQTQKEISELRYELERT---HQAKAEALVSREKNAIERLQK 225
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAERE---REIELQEKEAEREEAELEADVRKPAEAEKQaaeAEAEAEAEAIRAKGLAEAEGK 343
|
90 100
....*....|....*....|...
gi 2024343403 226 QQEIEAKEVYAQRQSLLKDIEVM 248
Cdd:COG2268 344 RALAEAWNKLGDAAILLMLIEKL 366
|
|
|